9G6V
Dissociated FMDV SAT2 Pentamer in complex with ultralong Fab117
This is a non-PDB format compatible entry.
Summary for 9G6V
| Entry DOI | 10.2210/pdb9g6v/pdb |
| EMDB information | 51105 |
| Descriptor | Genome polyprotein, Fab117 Heavy Chain, ... (4 entities in total) |
| Functional Keywords | disrupted, dissociated, vlp, internal epitope, pan-specific, ultralong, virus like particle |
| Biological source | Foot-and-mouth disease virus SAT 2 More |
| Total number of polymer chains | 20 |
| Total formula weight | 528297.59 |
| Authors | Clarke, J.D.,Duyvesteyn, H.M.E.,Ren, J.,Fry, E.E.,Owens, R.J.,Stuart, D.I.,Hammond, J.A. (deposition date: 2024-07-19, release date: 2024-10-30, Last modification date: 2024-11-20) |
| Primary citation | Clarke, J.D.,Duyvesteyn, H.M.E.,Perez-Martin, E.,Latisenko, U.,Porta, C.,Humphreys, K.V.,Hay, A.L.,Ren, J.,Fry, E.E.,van den Born, E.,Charleston, B.,Bonnet-Di Placido, M.,Owens, R.J.,Stuart, D.I.,Hammond, J.A. A broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids. J.Gen.Virol., 105:-, 2024 Cited by PubMed Abstract: Foot-and-mouth disease vaccination using inactivated virus is suboptimal, as the icosahedral viral capsids often disassemble into antigenically distinct pentameric units during long-term storage, or exposure to elevated temperature or lowered pH, and thus raise a response that is no longer protective. Furthermore, as foot-and-mouth disease virus (FMDV)'s seven serotypes are antigenically diverse, cross-protection from a single serotype vaccine is limited, and most existing mouse and bovine antibodies and camelid single-domain heavy chain-only antibodies are serotype-specific. For quality control purposes, there is a real need for pan-serotype antibodies that clearly distinguish between pentamer (12S) and protective intact FMDV capsid. To date, few cross-serotype bovine-derived antibodies have been reported in the literature. We identify a bovine antibody with an ultralong CDR-H3, Ab117, whose structural analysis reveals that it binds to a deep, hydrophobic pocket on the interior surface of the capsid via the CDR-H3. Main-chain and hydrophobic interactions provide broad serotype specificity. ELISA analysis confirms that Ab117 is a novel pan-serotype and conformational epitope-specific 12S reagent, suitable for assessing capsid integrity. PubMed: 39422666DOI: 10.1099/jgv.0.002032 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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